2RNM

Structure of The HET-s(218-289) prion in its amyloid form obtained by solid-state NMR

Summary for 2RNM

• Entry DOI: 10.2210/pdb2rnm/pdb
• Descriptor: Small s protein (1 entity in total)
• Functional Keywords: het-s(218-289), beta-solenoid, prion, amyloid fibril, parallel beta-sheets, hydrophobic core, salt bridges, asparagine ladders, beta-helix, protein fibril
• Biological source: Podospora anserina (Fungi)
• Cellular location: Cytoplasm: Q03689
• Total number of polymer chains: 5
• Total formula weight: 43338.25

Authors

Wasmer, C.,Lange, A.,Van Melckebeke, H.,Siemer, A.,Riek, R.,Meier, B.H. (deposition date: 2008-01-24, release date: 2008-04-01, Last modification date: 2024-05-01)

Primary citation

Wasmer, C.,Lange, A.,Van Melckebeke, H.,Siemer, A.B.,Riek, R.,Meier, B.H.
Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core
Science, 319:1523-1526, 2008

PubMed Abstract: Prion and nonprion forms of proteins are believed to differ solely in their three-dimensional structure, which is therefore of paramount importance for the prion function. However, no atomic-resolution structure of the fibrillar state that is likely infectious has been reported to date. We present a structural model based on solid-state nuclear magnetic resonance restraints for amyloid fibrils from the prion-forming domain (residues 218 to 289) of the HET-s protein from the filamentous fungus Podospora anserina. On the basis of 134 intra- and intermolecular experimental distance restraints, we find that HET-s(218-289) forms a left-handed beta solenoid, with each molecule forming two helical windings, a compact hydrophobic core, at least 23 hydrogen bonds, three salt bridges, and two asparagine ladders. The structure is likely to have broad implications for understanding the infectious amyloid state.

PubMed: 18339938
DOI: 10.1126/science.1151839

Experimental method

SOLUTION NMR